The Polyether Brevetoxins and Site Five of the Voltage-Sensitive Sodium Channel View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1990

AUTHORS

Daniel G. Baden

ABSTRACT

Florida red tide brevetoxins interact with a specific site associated with the voltage-sensitive sodium channel (VSSC) in a number of selected species. It is this same site which is involved in the molecular action of the marine polyether ciguatoxin. The site is located in a hydrophobic portion of the channel, the portion which is involved in activation/inactivation of ion flux across excitable membranes. Several different types of derivatized brevetoxins are available for investigation of sodium channel topography. Four tritiated brevetoxin probes, PbTx-3, PbTx-9, PbTx-7, and PbTx-10 are available for specific binding studies. In all cases, measurement of specific binding affinity and capacity parallels in vivo and in vitro potency. Dissociation constants are in the nanomolar concentration range, and binding maxima approximate 6–8 pmoles/mg protein. Brevetoxin photoaffinity probes bind in a specific covalent fashion to a protein component of approximately 260 kDa from synaptosomes, suggesting an association with the α-subunit of sodium channel. Bound toxin has been detected following polyacrylamide gel electrophoresis of sodium dodecylsulfate solubilized rat brain synaptosomes using: (1) goat antibrevetoxin-rabbit anti-goat-peroxidase sandwich immunoassays following Western blotting; (2) goat antibrevetoxin-peroxidase direct immunoassay; or (3) liquid scintillation detection of tritium-labeled brevetoxin photoaffinity probesodium channel conjugates. More... »

PAGES

545-551

Book

TITLE

Microbial Toxins in Foods and Feeds

ISBN

978-1-4612-7916-7
978-1-4613-0663-4

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4613-0663-4_50

DOI

http://dx.doi.org/10.1007/978-1-4613-0663-4_50

DIMENSIONS

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